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In order to study AT2mediated signal transduction mechanisms, two main approaches were used: (1) the ligandbinding properties of mutant AT2 receptors were characterized in comparison to wildtype after generation of a point mutation using sitedirected mutagenesis, and (2) interacting protein partners were analyzed using yeast library screening, coimmunoprecipitation and Western Blot studies. We found that the ability of Angiotensin II (Ang II) receptor type AT2 Phe308Ala residue mutant in the 7th TMD to bind peptidic ligands was greatly reduced, using Xenopus oocytes expression system. This residue occupies a position in the AT2 analogous to the Tyr292 in the AT1 essential for agonistic activation of that receptor. Screening of a 17day mouse embryo cDNA library with the Angiotensin II receptor AT2 as the bait in yeast twohybrid assay identified sodiumhydrogen exchanger NHE6 as the binding partner with 98% sequence homology. Further studies revealed that when human cellline MCF7 was transfected with the AT2, the AT2 coimmunoprecipitated with the NHE6 in the presence of Ang II, implying that Ang IImediated activation is needed for the interaction between AT2 and NHE6.
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